ID A0A1M7KLC0_9FLAO Unreviewed; 649 AA.
AC A0A1M7KLC0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:SHM66215.1};
GN ORFNames=SAMN05444484_10828 {ECO:0000313|EMBL:SHM66215.1};
OS Flavobacterium chilense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=946677 {ECO:0000313|EMBL:SHM66215.1, ECO:0000313|Proteomes:UP000184028};
RN [1] {ECO:0000313|EMBL:SHM66215.1, ECO:0000313|Proteomes:UP000184028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24724 {ECO:0000313|EMBL:SHM66215.1,
RC ECO:0000313|Proteomes:UP000184028};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; FRBT01000008; SHM66215.1; -; Genomic_DNA.
DR RefSeq; WP_068844685.1; NZ_LSYT01000010.1.
DR AlphaFoldDB; A0A1M7KLC0; -.
DR STRING; 946677.SAMN05444484_10828; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000184028; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR InterPro; IPR017790; Penicillin-binding_protein_2.
DR NCBIfam; TIGR03423; pbp2_mrdA; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Transferase {ECO:0000313|EMBL:SHM66215.1}.
FT DOMAIN 46..210
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 248..577
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 649 AA; 72963 MW; F4E27E18D41AEE78 CRC64;
MRKILLPSLI IIAASLLVIR IFYLQVVDDT FKLKSENNAI KKKYDYPERG YIYDRNGKLL
VANQASYDIM VIPREIKEDL NIGEFCALLN ITREDYDKRI AKAKVYSPRL PSVFLSQLNK
NEFAAFQEKI RKYEGFYFQK RSLRDYEVDY GANIFGFITQ VNERLIAKNP YYNSGDLIGQ
QGVEQSYEEI LRGVKGVKYI QKDKYNREIG SYKDGKYDTI AVAGEDINLT IDAELQKYGE
ELMINKRGGI VAIEPKSGEI LALVTAPSYD PGILVGRQRS KNYTLLYHDS IAKPLYDRGL
LAEYPPGSPF KILTGLVALQ EGVINEQTTF MCHHGFSYGR GRFMKCHGFG PHQLHNGIYN
SCNTYFAQSY MLTINKYKDP GKAVDVWSDH VKSFGLGQFM GYDLPIGKRG NIPNSKTYKK
IYPNGGWRST TIVSNAIGQG EVLMTPIQLA NMMATVANQG YYYTPHIIKK IEGKKIDAKF
TTKHVTTIDQ KYFPPVISGL FDVYNKGTAH ALRVEGIDIC GKTGTAENFA KINGKRTQLK
DHSIFVAFAP KDNPKIAIAI MIENGGFGAT VAGPIASLMI EKYLRKKITR TDLEIRVLNK
SLASEYAKLG GMNAASAIES TPKDSVMRAK ILKTKVEVKN TPIDTTKEN
//
